ID A0Y9Q8_9GAMM Unreviewed; 455 AA.
AC A0Y9Q8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Adenosylhomocysteinase {ECO:0000256|RuleBase:RU000548};
DE EC=3.13.2.1 {ECO:0000256|RuleBase:RU000548};
GN ORFNames=GP2143_16441 {ECO:0000313|EMBL:EAW32862.1};
OS marine gamma proteobacterium HTCC2143.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; BD1-7 clade.
OX NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW32862.1, ECO:0000313|Proteomes:UP000004931};
RN [1] {ECO:0000313|EMBL:EAW32862.1, ECO:0000313|Proteomes:UP000004931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW32862.1,
RC ECO:0000313|Proteomes:UP000004931};
RX PubMed=20601481; DOI=10.1128/JB.00683-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT isolated from the Oregon Coast.";
RL J. Bacteriol. 192:4530-4531(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC Evidence={ECO:0000256|RuleBase:RU000548};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRSR:PIRSR001109-2,
CC ECO:0000256|RuleBase:RU000548};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRSR:PIRSR001109-2,
CC ECO:0000256|RuleBase:RU000548};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000256|RuleBase:RU000548}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122, ECO:0000256|RuleBase:RU004166}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAW32862.1}.
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DR EMBL; AAVT01000001; EAW32862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Y9Q8; -.
DR STRING; 247633.GP2143_16441; -.
DR eggNOG; COG0499; Bacteria.
DR OrthoDB; 9802717at2; -.
DR UniPathway; UPA00314; UER00076.
DR Proteomes; UP000004931; Unassembled WGS sequence.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:RHEA.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR InterPro; IPR000043; Adenosylhomocysteinase-like.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR NCBIfam; TIGR00936; ahcY; 1.
DR PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU000548, ECO:0000313|EMBL:EAW32862.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR001109-2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000548};
KW Reference proteome {ECO:0000313|Proteomes:UP000004931}.
FT DOMAIN 191..367
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 157..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-1"
FT BINDING 222..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 313..315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 361
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
FT BINDING 368
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR001109-2"
SQ SEQUENCE 455 AA; 50344 MW; D6AE1DF7C2C15E58 CRC64;
MTTDYKVADI SLADWGRKEL NIAETEMPAL MAMRAKYRAS KPLAGAKILG CIHMTIQTGV
LIETLMELGA EVRWSSCNIF STQDHAAAAI AAAGVAVYAW KGETEEEYDW CLEQTILSDG
KPWDANMVLD DGGDLTLMLH QKFPEMLHKI HGVTEETTTG VHRLQEMLDS GELKIPAVNV
NDSVTKSKND NKYGCRHSLS DAIKRGTDHL MAGKKALVIG YGDVGKGSAQ SLRQEGMIVK
ITEIDPICAM QACMDGFEIV SPYNDGINTG KVEDTNKSLL QNTDLVVTTT GNFNVCDSAI
LRSLKNGAVV CNIGHFDNEI DTEYMRKNWE WEEVKPQVHT VYRDRASNDH LILLSEGRLV
NLGNATGHPS RIMDGSFANQ VLAQIYLYER KFADLEDNIK IDSITLEVLP KSLDEEVAAH
MVRGFGGVIT QLTQEQANYI NVSVEGPFKV DSYKY
//
